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Entry: A0A1G6ZT61_9PROT
LinkDB: A0A1G6ZT61_9PROT
Original site: A0A1G6ZT61_9PROT 
ID   A0A1G6ZT61_9PROT        Unreviewed;       420 AA.
AC   A0A1G6ZT61;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   05-JUN-2019, entry version 11.
DE   RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex {ECO:0000256|RuleBase:RU361138};
DE            EC=2.3.1.61 {ECO:0000256|RuleBase:RU361138};
DE   AltName: Full=2-oxoglutarate dehydrogenase complex component E2 {ECO:0000256|RuleBase:RU361138};
GN   ORFNames=SAMN04488071_1934 {ECO:0000313|EMBL:SDE05583.1};
OS   Kordiimonas lacus.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Kordiimonadales;
OC   Kordiimonadaceae; Kordiimonas.
OX   NCBI_TaxID=637679 {ECO:0000313|EMBL:SDE05583.1, ECO:0000313|Proteomes:UP000183685};
RN   [1] {ECO:0000313|EMBL:SDE05583.1, ECO:0000313|Proteomes:UP000183685}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 1.9109 {ECO:0000313|EMBL:SDE05583.1,
RC   ECO:0000313|Proteomes:UP000183685};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: E2 component of the 2-oxoglutarate dehydrogenase (OGDH)
CC       complex which catalyzes the second step in the conversion of 2-
CC       oxoglutarate to succinyl-CoA and CO(2).
CC       {ECO:0000256|RuleBase:RU361138}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-dihydrolipoyl-L-lysyl-[2-oxoglutarate
CC         dehydrogenase complex component E2] + succinyl-CoA = (R)-N(6)-
CC         (S(8)-succinyldihydrolipoyl)-L-lysyl-[2-oxoglutarate
CC         dehydrogenase complex component E2] + CoA; Xref=Rhea:RHEA:15213,
CC         Rhea:RHEA-COMP:10581, Rhea:RHEA-COMP:10582, ChEBI:CHEBI:57287,
CC         ChEBI:CHEBI:57292, ChEBI:CHEBI:83100, ChEBI:CHEBI:83120;
CC         EC=2.3.1.61; Evidence={ECO:0000256|RuleBase:RU361138};
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|RuleBase:RU361138};
CC       Note=Binds 1 lipoyl cofactor covalently.
CC       {ECO:0000256|RuleBase:RU361138};
CC   -!- PATHWAY: Amino-acid degradation; L-lysine degradation via
CC       saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.
CC       {ECO:0000256|RuleBase:RU361138}.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC       {ECO:0000256|RuleBase:RU361138}.
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DR   EMBL; FNAK01000004; SDE05583.1; -; Genomic_DNA.
DR   RefSeq; WP_068304316.1; NZ_LRUA01000003.1.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000183685; Unassembled WGS sequence.
DR   GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniRule.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.559.10; -; 1.
DR   Gene3D; 4.10.320.10; -; 1.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR036625; E3-bd_dom_sf.
DR   InterPro; IPR004167; PSBD.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   InterPro; IPR006255; SucB.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   TIGRFAMs; TIGR01347; sucB; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
DR   PROSITE; PS51826; PSBD; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000256|RuleBase:RU361138};
KW   Complete proteome {ECO:0000313|Proteomes:UP000183685};
KW   Lipoyl {ECO:0000256|RuleBase:RU361138, ECO:0000256|SAAS:SAAS00065550};
KW   Reference proteome {ECO:0000313|Proteomes:UP000183685};
KW   Transferase {ECO:0000256|RuleBase:RU361138};
KW   Tricarboxylic acid cycle {ECO:0000256|RuleBase:RU361138}.
FT   DOMAIN        3     78       Lipoyl-binding. {ECO:0000259|PROSITE:
FT                                PS50968}.
FT   DOMAIN      130    167       Peripheral subunit-binding (PSBD).
FT                                {ECO:0000259|PROSITE:PS51826}.
FT   REGION       80    128       Disordered. {ECO:0000256|MobiDB-lite:
FT                                A0A1G6ZT61}.
SQ   SEQUENCE   420 AA;  44542 MW;  7A5C5837A968A9B4 CRC64;
     MAIEDIVIPQ MGESVAEGTI GTWLKKVGDA VAADEPIVEV ETDKVAMEVP SPVAGVLVEI
     VAEEGQDVEI GALIAKVDTE GKASSGGSGD SKPAAKKEEA AAPAAKKEEA APAPSPAPAS
     QGAPAKDLMP MSPAVRRIVQ DYNLDPSSIT GTGKDGRLTK GDVMSAIESG SARTLDVLPA
     SAAAAPAGPR EERVKMTRLR KKIAERLKDA QNTAAMLTTY NEVDMSAVMA ARNKYKDLFA
     RKHNIKLGFM SFFTKACCLA LKEIPAVNAQ IEGDEIVYHN FANIGVAVSS PNGLVVPVLK
     DAQNMSFADT ELSIANFGKK ARDGKLTIDD MQGGTFTISN GGIFGSLMSS PILNAPQSGI
     LGMHKIQERP VVENGQVVIR PMMYLALSYD HRIIDGREAV TFLVRVKEAL EDPTRLLLDM
//
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